The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Protein N-Glycosylation, Protein Folding, and Protein Quality Control
Open accessAbstract
Quality control of protein folding represents a fundamental cellular activity. Early steps of protein N-glycosylation involving the removal of three glucose and some specific mannose residues in the endoplasmic reticulum have been recognized as being of importance for protein quality control. Specific oligosaccharide structures resulting from the oligosaccharide processing may represent a glycocode promoting productive protein folding, whereas others may represent glyco-codes for routing not correctly folded proteins for dislocation from the endoplasmic reticulum to the cytosol and subsequent degradation. Although quality control of protein folding is essential for the proper functioning of cells, it is also the basis for protein folding disorders since the recognition and elimination of non-native conformers can result either in loss-of-function or pathological-gain-of-function. The machinery for protein folding control represents a prime example of an intricate interactome present in a single organelle, the endoplasmic reticulum. Here, current views of mechanisms for the recognition and retention leading to productive protein folding or the eventual elimination of misfolded glycoproteins in yeast and mammalian cells are reviewed.
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Cites
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Self-citationDefining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation
Quan, E. M., Kamiya, Y., Kamiya, D., Denic, V., Weibezahn, J., Kato, K., & Weissman, J. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.017 · Cited by 242
Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M., & Helenius, A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00494-5 · Cited by 221
Pelletier, M. F., Marcil, A., Sevigny, G., Jakob, C. A., Tessier, D. C., Chevet, E., Menard, R., Bergeron, J. J. M., & Thomas, D. Y. (2000) · Glycobiology · doi:10.1093/glycob/10.8.815 · Cited by 123
Cited by
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Endoplasmic Reticulum Stress: Its Role in Disease and Novel Prospects for Therapy
Schönthal, A. H. (2012) · Scientifica · doi:10.6064/2012/857516 · Cited by 353
Pekkala, S., Wiklund, P. K., Hulmi, J. J., Ahtiainen, J. P., Horttanainen, M., Pöllänen, E., Mäkelä, K. A., Kainulainen, H., Häkkinen, K., Nyman, K., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.263707 · Cited by 292
Garrido, D., Nwosu, C., Ruiz-Moyano, S., Aldredge, D., German, J. B., Lebrilla, C. B., & Mills, D. A. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.018119 · Cited by 150
Current advances in the algae-made biopharmaceuticals field
Rosales-Mendoza, S., Solís-Andrade, K. I., Márquez-Escobar, V. A., González-Ortega, O., & Bañuelos-Hernandez, B. (2020) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2020.1739643 · Cited by 55
Metadata
- Authors
- Roth, J., Zuber, C., Park, S., Jang, I., Lee, Y., Kysela, K. G., Fourn, V. L., Santimaria, R., Guhl, B., & Cho, J. W.
- Venue
- Molecules and Cells
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 30
- Issue
- 6
- Pages
- 497-506
- ISSN
- 0219-1032 (ISSN-L)
- 1016-8478
- OpenAlex
- W2073592678
- Cited by
- 183
- References
- 6
- FWCI
- 4.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Roth, J., Zuber, C., Park, S., Jang, I., Lee, Y., Kysela, K. G., Fourn, V. L., Santimaria, R., Guhl, B., & Cho, J. W. (2010). Protein N-Glycosylation, Protein Folding, and Protein Quality Control. Molecules and Cells. https://doi.org/10.1007/s10059-010-0159-z
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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